Chromosomal proteins appear to have an important regulatory function in the control of transcription. The nonhistone proteins and their phosphorylated derivatives may serve as positive regulatory agents. Intrinsic nuclear protein kinases (and phosphatases) appear to be involved in these phosphorylation reactions. We have established that in the prostatic tissue these reactions are profoundly and rapidly influenced by the androgenic status of the animals. The importance of this observation on prostatic nuclear protein kinase activities is further underscored by our recent demonstration that androgen control of phosphorylation of prostatic nuclear matrix phosphoproteins is determined by the level of the endogenous protein kinase(s) rather than the amount of substrate. Of the seven nuclear protein kinases described by us, we have now partially purified two of the androgen-sensitive kinases. These were chosen because the loss of activity of these two enzymes is as rapid or even more rapid than the loss of nuclear androgen receptor. Our current effort is directed to achieve a higher purification of these enzymes. We will then attempt to raise antibodies against them. The availability of these antibodies should allow a more detailed analysis of the molecular biology of these enzymes in relation to mediation of androgen action. Our work on the polyamine stimulation of cAMP-independent protein kinase reactions has demonstrated that (1) prostatic spermine-binding protein is a phosphoprotein whose phosphorylation is mediated only by cAMP-independent protein kinase and is markedly enhanced by polyamines; and (2) of the various nuclear-associated proteins whose phosphorylation is affected by polyamines, it is the group that belongs to the neutral and basic nonhistones (identified by us) that is the most responsive to polyamines; this observation is of particular interest since these proteins have been implicated in the acceptor function for the androgen-receptor complex.